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Literature summary extracted from

  • Lee, D.C.; Cottrill, M.A.; Forsberg, C.W.; Jia, Z.
    Functional insights revealed by the crystal structures of Escherichia coli glucose-1-phosphatase (2003), J. Biol. Chem., 278, 31412-31418.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.3.10 determination of crystal structure by multiwavelength anomalous dispersion using a tungstate derivate together with the H18A inactive mutant complex structure with D-glucose 1-phosphate at 2.4 A resolution Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.10 0.39
-
D-glucose 1-phosphate pH 6.5 Escherichia coli
3.1.3.10 0.54
-
myo-inositol hexakisphosphate pH 4.5 Escherichia coli
3.1.3.10 1.6
-
D-glucose 6-phosphate
-
Escherichia coli
3.1.3.10 2.2
-
D-Fructose 1-phosphate
-
Escherichia coli
3.1.3.10 11
-
D-ribose 5-phosphate
-
Escherichia coli
3.1.3.10 13
-
p-nitrophenyl phosphate pH 3.5 Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.3.10 periplasm
-
Escherichia coli
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.3.10 D-glucose 6-phosphate + H2O Escherichia coli the enzyme acts as a D-glucose scavenger D-glucose + phosphate
-
?
3.1.3.10 myo-inositol hexakisphosphate + H2O Escherichia coli the enzyme is potentially involved in pathogenic inositol phosphate signal transduction pathways via type III secretioin into the host cell ? + phosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.10 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.10 D-glucose 1-phosphate + H2O
-
Escherichia coli D-glucose + phosphate
-
?
3.1.3.10 D-glucose 6-phosphate
-
Escherichia coli D-glucose + phosphate
-
?
3.1.3.10 D-glucose 6-phosphate + H2O
-
Escherichia coli D-glucose + phosphate
-
?
3.1.3.10 D-glucose 6-phosphate + H2O the enzyme acts as a D-glucose scavenger Escherichia coli D-glucose + phosphate
-
?
3.1.3.10 D-ribose 5-phosphate
-
Escherichia coli D-ribose + phosphate
-
?
3.1.3.10 fructose 1-phosphate
-
Escherichia coli fructose + phosphate
-
?
3.1.3.10 myo-inositol hexakisphosphate + H2O
-
Escherichia coli ? + phosphate
-
?
3.1.3.10 myo-inositol hexakisphosphate + H2O the enzyme is potentially involved in pathogenic inositol phosphate signal transduction pathways via type III secretioin into the host cell Escherichia coli ? + phosphate
-
?
3.1.3.10 p-nitrophenyl phosphate
-
Escherichia coli p-nitrophenol + phosphate
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.3.10 3 6 p-nitrophenyl phosphate pH 3.5 Escherichia coli
3.1.3.10 12
-
myo-inositol hexakisphosphate pH 4.5 Escherichia coli
3.1.3.10 42
-
D-ribose 5-phosphate
-
Escherichia coli
3.1.3.10 82
-
D-glucose 6-phosphate
-
Escherichia coli
3.1.3.10 95
-
D-Fructose 1-phosphate
-
Escherichia coli
3.1.3.10 117
-
D-glucose 1-phosphate pH 6.5 Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.10 3.5
-
p-nitrophenyl phosphate as substrate Escherichia coli
3.1.3.10 4.5
-
myo-inositol hexakisphophate as substrate Escherichia coli
3.1.3.10 6.5
-
D-glucose 1-phosphate as substrate Escherichia coli

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.3.10 2.5 9.5 D-glucose 1-phosphate as substrate Escherichia coli
3.1.3.10 3 7 myo-inositol hexakisphophate as substrate Escherichia coli
3.1.3.10 3 6.5 p-nitrophenyl phosphate as substrate Escherichia coli